کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5512167 | 1540222 | 2017 | 7 صفحه PDF | دانلود رایگان |
The equilibrium isotherms and adsorption kinetics of lysozyme (LZ) on epichlorohydrin (Epi) cross-linked alginate-guar gum (Alg-GG) matrix were studied. Adsorption kinetics followed a pseudo-first-order model while the equilibrium isotherm could be represented by the Freundlich equation. The maximal amount of LZ adsorbed onto this matrix was around 2.4Â mg per g of hydrated matrix at pH 7.00. The adsorption mechanism was associated to a simple diffusion process with a weak columbic interaction between LZ and the matrix. The presence of NaCl 0.3Â M induced a total displacement of the LZ from the matrix. Under this condition, the percentage of desorbed protein was 95%. Successive cycles of adsorption-washing-elution were performed and the results showed the reversibility of the process and the usefulness of the method for enzyme purification and separation. A last successful step was carried out for the purification of LZ from egg white as natural source. The model proved to be useful applied as a platform design in the isolation and purification of proteins.
Journal: International Journal of Biological Macromolecules - Volume 96, March 2017, Pages 111-117